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| | ==4.3A resolution structure of a MinD-MinE(I24N) protein complex== | | ==4.3A resolution structure of a MinD-MinE(I24N) protein complex== |
| - | <StructureSection load='3r9j' size='340' side='right' caption='[[3r9j]], [[Resolution|resolution]] 4.30Å' scene=''> | + | <StructureSection load='3r9j' size='340' side='right'caption='[[3r9j]], [[Resolution|resolution]] 4.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3r9j]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R9J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3r9j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R9J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q9l|3q9l]], [[3r9i|3r9i]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3q9l|3q9l]], [[3r9i|3r9i]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1175, JW1164, minD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b1174, JW1163, minE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1175, JW1164, minD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b1174, JW1163, minE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r9j OCA], [http://pdbe.org/3r9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r9j RCSB], [http://www.ebi.ac.uk/pdbsum/3r9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r9j ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r9j OCA], [https://pdbe.org/3r9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r9j RCSB], [https://www.ebi.ac.uk/pdbsum/3r9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r9j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref> [[http://www.uniprot.org/uniprot/MINE_ECOLI MINE_ECOLI]] Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.<ref>PMID:22380631</ref> | + | [[https://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref> [[https://www.uniprot.org/uniprot/MINE_ECOLI MINE_ECOLI]] Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.<ref>PMID:22380631</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Ecoli]] | | [[Category: Ecoli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Battaile, K P]] | | [[Category: Battaile, K P]] |
| | [[Category: Holyoak, T]] | | [[Category: Holyoak, T]] |
| Structural highlights
3r9j is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Related: | |
| Gene: | b1175, JW1164, minD (ECOLI), b1174, JW1163, minE (ECOLI) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[MIND_ECOLI] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.[1] [2] [MINE_ECOLI] Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.[3]
Publication Abstract from PubMed
In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear because the MinD-binding regions of MinE are sequestered within a six-stranded beta sheet and masked by N-terminal helices. minE mutations that restore interaction between some MinD and MinE mutants were isolated. These mutations alter the MinE structure leading to release of the MinD-binding regions and the N-terminal helices that bind the membrane. Crystallization of MinD-MinE complexes revealed a four-stranded beta sheet MinE dimer with the released beta strands (MinD-binding regions) converted to alpha helices bound to MinD dimers. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface. PAPERFLICK:
The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.,Park KT, Wu W, Battaile KP, Lovell S, Holyoak T, Lutkenhaus J Cell. 2011 Aug 5;146(3):396-407. PMID:21816275[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ de Boer PA, Crossley RE, Hand AR, Rothfield LI. The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site. EMBO J. 1991 Dec;10(13):4371-80. PMID:1836760
- ↑ Li G, Young KD. Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol Microbiol. 2012 Apr;84(2):276-95. doi: 10.1111/j.1365-2958.2012.08021.x. Epub, 2012 Mar 8. PMID:22380631 doi:10.1111/j.1365-2958.2012.08021.x
- ↑ Li G, Young KD. Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol Microbiol. 2012 Apr;84(2):276-95. doi: 10.1111/j.1365-2958.2012.08021.x. Epub, 2012 Mar 8. PMID:22380631 doi:10.1111/j.1365-2958.2012.08021.x
- ↑ Park KT, Wu W, Battaile KP, Lovell S, Holyoak T, Lutkenhaus J. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. Cell. 2011 Aug 5;146(3):396-407. PMID:21816275 doi:10.1016/j.cell.2011.06.042
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